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Conserved domains on  [gi|148728385|gb|ABR08667|]
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cytochrome oxidase subunit II, partial (mitochondrion) [Mecopoda elongata]

Protein Classification

cytochrome c oxidase subunit II( domain architecture ID 11475927)

cytochrome c oxidase subunit II, part of the functional core of the enzyme, transfers the electrons from cytochrome c via its binuclear copper A center to the bimetallic center of the catalytic subunit I

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
COX2 MTH00154
cytochrome c oxidase subunit II; Provisional
 1-173 3.66e-107

cytochrome c oxidase subunit II; Provisional


:

Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 305.60  E-value: 3.66e-107
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148728385   1 TLLILVMITILVAYIMTAIMLYSFTHRYLLEGQLIELIWTILPAMTLIFIALPSLRLLYLLDDTVDPSISLKTVGHQWYW 80
Cdd:MTH00154  27 TMMILIMITILVGYMMISLLFNKFTNRFLLEGQEIEIIWTILPAIILIFIALPSLRLLYLLDEVNNPSITLKTIGHQWYW 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148728385  81 SYEYTDFVNpYEFDSYMIPYNEMNSDGFRLLDVDNRTILPFHTQVRMMVTAADVLHSWTIPALGVKVDATPGRLNQTNFF 160
Cdd:MTH00154 107 SYEYSDFKN-IEFDSYMIPTNELENNGFRLLDVDNRLVLPMNTQIRILITAADVIHSWTVPSLGVKVDAVPGRLNQLNFL 185

                        170
                 ....*....|...
gi 148728385 161 INRPGTYYGQCSE 173
Cdd:MTH00154 186 INRPGLFFGQCSE 198
 
Name Accession Description Interval E-value
COX2 MTH00154
cytochrome c oxidase subunit II; Provisional
 1-173 3.66e-107

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 305.60  E-value: 3.66e-107
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148728385   1 TLLILVMITILVAYIMTAIMLYSFTHRYLLEGQLIELIWTILPAMTLIFIALPSLRLLYLLDDTVDPSISLKTVGHQWYW 80
Cdd:MTH00154  27 TMMILIMITILVGYMMISLLFNKFTNRFLLEGQEIEIIWTILPAIILIFIALPSLRLLYLLDEVNNPSITLKTIGHQWYW 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148728385  81 SYEYTDFVNpYEFDSYMIPYNEMNSDGFRLLDVDNRTILPFHTQVRMMVTAADVLHSWTIPALGVKVDATPGRLNQTNFF 160
Cdd:MTH00154 107 SYEYSDFKN-IEFDSYMIPTNELENNGFRLLDVDNRLVLPMNTQIRILITAADVIHSWTVPSLGVKVDAVPGRLNQLNFL 185

                        170
                 ....*....|...
gi 148728385 161 INRPGTYYGQCSE 173
Cdd:MTH00154 186 INRPGLFFGQCSE 198
CcO_II_C cd13912
C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ...
 67-173 9.90e-67

C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal oxidase in the respiratory chains of eukaryotes and most bacteria, is a multi-chain transmembrane protein located in the inner membrane of mitochondria and the cell membrane of prokaryotes. It catalyzes the reduction of O2 and simultaneously pumps protons across the membrane. The number of subunits varies from three to five in bacteria and up to 13 in mammalian mitochondria. Only subunits I and II are essential for function. Subunits I, II, and III of mammalian CcO are encoded within the mitochondrial genome and the remaining 10 subunits are encoded within the nuclear genome. Subunit II contains a copper-copper binuclear site called CuA, which is believed to be involved in electron transfer from cytochrome c to the binuclear center (active site) in subunit I.


Pssm-ID: 259979 [Multi-domain]  Cd Length: 130  Bit Score: 199.72  E-value: 9.90e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148728385  67 PSISLKTVGHQWYWSYEYTDFvNPYEFDSYMIPYNEMNSDGFRLLDVDNRTILPFHTQVRMMVTAADVLHSWTIPALGVK 146
Cdd:cd13912    1 PSLTIKAIGHQWYWSYEYSDF-NDLEFDSYMIPEDDLEKGQLRLLEVDNRLVVPVNTHIRVLVTSADVIHSWAVPSLGIK 79

                         90       100
                 ....*....|....*....|....*..
gi 148728385 147 VDATPGRLNQTNFFINRPGTYYGQCSE 173
Cdd:cd13912   80 VDAVPGRLNQTSFFIERPGVYYGQCSE 106
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
69-173 5.73e-60

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 182.22  E-value: 5.73e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148728385   69 ISLKTVGHQWYWSYEYTDFVNpYEFDSYMIPYNEMNSDGFRLLDVDNRTILPFHTQVRMMVTAADVLHSWTIPALGVKVD 148
Cdd:pfam00116   1 LTIKAIGHQWYWSYEYTDFGD-LEFDSYMIPTEDLEEGQLRLLEVDNRVVLPVETHIRVIVTAADVIHSWAVPSLGIKTD 79

                          90       100
                  ....*....|....*....|....*
gi 148728385  149 ATPGRLNQTNFFINRPGTYYGQCSE 173
Cdd:pfam00116  80 AVPGRLNQTSFSIDREGVFYGQCSE 104
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
1-174 3.38e-34

Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 119.93  E-value: 3.38e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148728385   1 TLLILVMITILVAyIMTAIMLYSFTHR-------YLLEGQLIELIWTILPAMTLIFIALPSLRLLYLLDDTVDPSISLKT 73
Cdd:COG1622   39 SLIIMLVIFVLVF-GLLLYFAIRYRRRkgdadpaQFHHNTKLEIVWTVIPIIIVIVLAVPTLRVLHALDDAPEDPLTVEV 117

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148728385  74 VGHQWYWSYEYTDfvnpyefdsymipYNEmnsdgfrllDVDNRTILPFHTQVRMMVTAADVLHSWTIPALGVKVDATPGR 153
Cdd:COG1622  118 TGYQWKWLFRYPD-------------QGI---------ATVNELVLPVGRPVRFLLTSADVIHSFWVPALGGKQDAIPGR 175

                        170       180
                 ....*....|....*....|.
gi 148728385 154 LNQTNFFINRPGTYYGQCSEF 174
Cdd:COG1622  176 VTELWFTADKPGTYRGQCAEL 196
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 2-174 2.99e-25

cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of mitochondria (and one of several possible acceptors in prokaryotes) in the electron transport chain of aerobic respiration. The enzyme couples the oxidation of reduced cytochrome c with the reduction of molecular oxygen to water. This process results in the pumping of four protons across the membrane which are used in the proton gradient powered synthesis of ATP. The oxidase contains two heme a cofactors and three copper atoms as well as other bound ions. [Energy metabolism, Electron transport]


Pssm-ID: 274329 [Multi-domain]  Cd Length: 199  Bit Score: 96.30  E-value: 2.99e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148728385    2 LLILVMITILVayIMTAIMLYS-FTHR---------YLLEGQLIELIWTILPA-MTLIFIALPSLRLLYLLDDTVDPSIS 70
Cdd:TIGR02866  15 FVLAVSTLISL--LVAALLAYVvWKFRrkgdeekpsQIHGNRRLEYVWTVIPLiIVVGLFAATAKGLLYLERPIPKDALK 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148728385   71 LKTVGHQWYWSYEYTDFvnpyefdsymipynemnsdGFRlldVDNRTILPFHTQVRMMVTAADVLHSWTIPALGVKVDAT 150
Cdd:TIGR02866  93 VKVTGYQWWWDFEYPES-------------------GFT---TVNELVLPAGTPVELQVTSKDVIHSFWVPELGGKIDAI 150

                         170       180
                  ....*....|....*....|....
gi 148728385  151 PGRLNQTNFFINRPGTYYGQCSEF 174
Cdd:TIGR02866 151 PGQTNALWFNADEPGVYYGFCAEL 174
 
Name Accession Description Interval E-value
COX2 MTH00154
cytochrome c oxidase subunit II; Provisional
 1-173 3.66e-107

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 305.60  E-value: 3.66e-107
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148728385   1 TLLILVMITILVAYIMTAIMLYSFTHRYLLEGQLIELIWTILPAMTLIFIALPSLRLLYLLDDTVDPSISLKTVGHQWYW 80
Cdd:MTH00154  27 TMMILIMITILVGYMMISLLFNKFTNRFLLEGQEIEIIWTILPAIILIFIALPSLRLLYLLDEVNNPSITLKTIGHQWYW 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148728385  81 SYEYTDFVNpYEFDSYMIPYNEMNSDGFRLLDVDNRTILPFHTQVRMMVTAADVLHSWTIPALGVKVDATPGRLNQTNFF 160
Cdd:MTH00154 107 SYEYSDFKN-IEFDSYMIPTNELENNGFRLLDVDNRLVLPMNTQIRILITAADVIHSWTVPSLGVKVDAVPGRLNQLNFL 185

                        170
                 ....*....|...
gi 148728385 161 INRPGTYYGQCSE 173
Cdd:MTH00154 186 INRPGLFFGQCSE 198
COX2 MTH00139
cytochrome c oxidase subunit II; Provisional
 1-173 2.44e-82

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214429 [Multi-domain]  Cd Length: 226  Bit Score: 242.70  E-value: 2.44e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148728385   1 TLLILVMITILVAYIMTAIMLYSFTHRYLLEGQLIELIWTILPAMTLIFIALPSLRLLYLLDDTVDPSISLKTVGHQWYW 80
Cdd:MTH00139  27 AMVILIMILSFVGYISLSLMSNKFTSRSLLESQEVETIWTVLPAFILLFLALPSLRLLYLMDEVSDPYLTFKAVGHQWYW 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148728385  81 SYEYTDFVNpYEFDSYMIPYNEMNSDGFRLLDVDNRTILPFHTQVRMMVTAADVLHSWTIPALGVKVDATPGRLNQTNFF 160
Cdd:MTH00139 107 SYEYSDFKN-LSFDSYMIPTEDLSSGEFRLLEVDNRLVLPYKSNIRALITAADVLHSWTVPSLGVKIDAVPGRLNQVGFF 185

                        170
                 ....*....|...
gi 148728385 161 INRPGTYYGQCSE 173
Cdd:MTH00139 186 INRPGVFYGQCSE 198
COX2 MTH00140
cytochrome c oxidase subunit II; Provisional
 1-173 3.60e-82

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214430 [Multi-domain]  Cd Length: 228  Bit Score: 242.15  E-value: 3.60e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148728385   1 TLLILVMITILVAYIMTAIMLYSFTHRYLLEGQLIELIWTILPAMTLIFIALPSLRLLYLLDDTVDPSISLKTVGHQWYW 80
Cdd:MTH00140  27 AMVVLVLIFSFVMYMLVLLLFNKFSCRTILEAQKLETIWTIVPALILVFLALPSLRLLYLLDETNNPLLTVKAIGHQWYW 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148728385  81 SYEYTDFVNpYEFDSYMIPYNEMNSDGFRLLDVDNRTILPFHTQVRMMVTAADVLHSWTIPALGVKVDATPGRLNQTNFF 160
Cdd:MTH00140 107 SYEYSDFSV-IEFDSYMVPENELELGDFRLLEVDNRLVLPYSVDTRVLVTSADVIHSWTVPSLGVKVDAIPGRLNQLSFE 185

                        170
                 ....*....|...
gi 148728385 161 INRPGTYYGQCSE 173
Cdd:MTH00140 186 PKRPGVFYGQCSE 198
COX2 MTH00008
cytochrome c oxidase subunit II; Validated
 1-173 5.89e-79

cytochrome c oxidase subunit II; Validated


Pssm-ID: 164584 [Multi-domain]  Cd Length: 228  Bit Score: 234.37  E-value: 5.89e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148728385   1 TLLILVMITILVAYIMTAIMLYSFTHRYLLEGQLIELIWTILPAMTLIFIALPSLRLLYLLDDTVDPSISLKTVGHQWYW 80
Cdd:MTH00008  27 ALLILTLVLTVVGYAMTSLMFNKLSNRYILEAQQIETIWTILPALILLFLAFPSLRLLYLMDEVSNPSITLKTIGHQWYW 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148728385  81 SYEYTDFVNpYEFDSYMIPYNEMNSDGFRLLDVDNRTILPFHTQVRMMVTAADVLHSWTIPALGVKVDATPGRLNQTNFF 160
Cdd:MTH00008 107 SYEYSDFSN-LEFDSYMLPTSDLSPGQFRLLEVDNRAVLPMQTEIRVLVTAADVIHSWTVPSLGVKVDAVPGRLNQIGFT 185

                        170
                 ....*....|...
gi 148728385 161 INRPGTYYGQCSE 173
Cdd:MTH00008 186 ITRPGVFYGQCSE 198
COX2 MTH00168
cytochrome c oxidase subunit II; Provisional
 1-173 6.26e-79

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177223 [Multi-domain]  Cd Length: 225  Bit Score: 234.10  E-value: 6.26e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148728385   1 TLLILVMITILVAYIMTAIMLYSFTHRYLLEGQLIELIWTILPAMTLIFIALPSLRLLYLLDDTVDPSISLKTVGHQWYW 80
Cdd:MTH00168  27 ALLILVLILTLVLYSLLVLVTSKYTNRFLLDSQMIEFVWTIIPAFILISLALPSLRLLYLMDEIDKPDLTIKAVGHQWYW 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148728385  81 SYEYTDFVNpYEFDSYMIPYNEMNSDGFRLLDVDNRTILPFHTQVRMMVTAADVLHSWTIPALGVKVDATPGRLNQTNFF 160
Cdd:MTH00168 107 SYEYTDYND-LEFDSYMVPTQDLSPGQFRLLEVDNRLVLPMDSKIRVLVTSADVLHSWTLPSLGLKMDAVPGRLNQLAFL 185

                        170
                 ....*....|...
gi 148728385 161 INRPGTYYGQCSE 173
Cdd:MTH00168 186 SSRPGSFYGQCSE 198
COX2 MTH00117
cytochrome c oxidase subunit II; Provisional
 1-173 3.34e-78

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177178 [Multi-domain]  Cd Length: 227  Bit Score: 232.11  E-value: 3.34e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148728385   1 TLLILVMITILVAYIMTAIMLYSFTHRYLLEGQLIELIWTILPAMTLIFIALPSLRLLYLLDDTVDPSISLKTVGHQWYW 80
Cdd:MTH00117  27 ALMVALLISSLVLYLLTLMLTTKLTHTNTVDAQEVELIWTILPAIVLILLALPSLRILYLMDEINNPHLTIKAIGHQWYW 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148728385  81 SYEYTDFVNpYEFDSYMIPYNEMNSDGFRLLDVDNRTILPFHTQVRMMVTAADVLHSWTIPALGVKVDATPGRLNQTNFF 160
Cdd:MTH00117 107 SYEYTDYKD-LSFDSYMIPTQDLPNGHFRLLEVDHRMVIPMESPIRILITAEDVLHSWAVPSLGVKTDAVPGRLNQTSFI 185

                        170
                 ....*....|...
gi 148728385 161 INRPGTYYGQCSE 173
Cdd:MTH00117 186 TTRPGVFYGQCSE 198
COX2 MTH00038
cytochrome c oxidase subunit II; Provisional
 1-173 1.41e-77

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177113 [Multi-domain]  Cd Length: 229  Bit Score: 230.74  E-value: 1.41e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148728385   1 TLLILVMITILVAYIMTAIMLYSFTHRYLLEGQLIELIWTILPAMTLIFIALPSLRLLYLLDDTVDPSISLKTVGHQWYW 80
Cdd:MTH00038  27 ALIILTLITILVFYGLASLLFSSPTNRFFLEGQELETIWTIVPAFILIFIALPSLQLLYLMDEVNNPFLTIKAIGHQWYW 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148728385  81 SYEYTDFvNPYEFDSYMIPYNEMNSDGFRLLDVDNRTILPFHTQVRMMVTAADVLHSWTIPALGVKVDATPGRLNQTNFF 160
Cdd:MTH00038 107 SYEYTDY-NDLEFDSYMVPTSDLSTGLPRLLEVDNRLVLPYQTPIRVLVSSADVLHSWAVPSLGVKMDAVPGRLNQTTFF 185

                        170
                 ....*....|...
gi 148728385 161 INRPGTYYGQCSE 173
Cdd:MTH00038 186 ISRTGLFYGQCSE 198
COX2 MTH00023
cytochrome c oxidase subunit II; Validated
 2-173 1.88e-73

cytochrome c oxidase subunit II; Validated


Pssm-ID: 214402 [Multi-domain]  Cd Length: 240  Bit Score: 220.78  E-value: 1.88e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148728385   2 LLILVMITILVAYIMTAIMLYSFTHRYLLEGQLIELIWTILPAMTLIFIALPSLRLLYLLDDTVDPSISLKTVGHQWYWS 81
Cdd:MTH00023  37 MFLLIIIITVVLWLIVEALNGKFYDRFLVDGTFLEIVWTIIPAVILVFIALPSLKLLYLMDEVVSPALTIKAIGHQWYWS 116

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148728385  82 YEYTDFVNP-YEFDSYMIPYNEMNSDGFRLLDVDNRTILPFHTQVRMMVTAADVLHSWTIPALGVKVDATPGRLNQTNFF 160
Cdd:MTH00023 117 YEYSDYEGEtLEFDSYMVPTSDLNSGDFRLLEVDNRLVVPINTHVRILVTGADVLHSFAVPSLGLKIDAVPGRLNQTGFF 196

                        170
                 ....*....|...
gi 148728385 161 INRPGTYYGQCSE 173
Cdd:MTH00023 197 IKRPGVFYGQCSE 209
COX2 MTH00051
cytochrome c oxidase subunit II; Provisional
 2-173 1.04e-72

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177126 [Multi-domain]  Cd Length: 234  Bit Score: 218.50  E-value: 1.04e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148728385   2 LLILVMITILVAYIMTAIMLYSFTHRYLLEGQLIELIWTILPAMTLIFIALPSLRLLYLLDDTVDPSISLKTVGHQWYWS 81
Cdd:MTH00051  30 MFILTIIITTVLWLIIRALTTKYYHKYLFEGTLIEIIWTLIPAAILIFIAFPSLKLLYLMDEVIDPALTIKAIGHQWYWS 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148728385  82 YEYTDF-VNPYEFDSYMIPYNEMNSDGFRLLDVDNRTILPFHTQVRMMVTAADVLHSWTIPALGVKVDATPGRLNQTNFF 160
Cdd:MTH00051 110 YEYSDYgTDTIEFDSYMIPTSDLNSGDLRLLEVDNRLIVPIQTQVRVLVTAADVLHSFAVPSLSVKIDAVPGRLNQTSFF 189

                        170
                 ....*....|...
gi 148728385 161 INRPGTYYGQCSE 173
Cdd:MTH00051 190 IKRPGVFYGQCSE 202
COX2 MTH00185
cytochrome c oxidase subunit II; Provisional
 1-173 5.83e-71

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164736 [Multi-domain]  Cd Length: 230  Bit Score: 213.98  E-value: 5.83e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148728385   1 TLLILVMITILVAYIMTAIMLYSFTHRYLLEGQLIELIWTILPAMTLIFIALPSLRLLYLLDDTVDPSISLKTVGHQWYW 80
Cdd:MTH00185  27 TLMIVFLISTLVLYIIVAMVTTKLTNKYILDSQEIEIVWTILPAIILIMIALPSLRILYLMDEINDPHLTIKAMGHQWYW 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148728385  81 SYEYTDFvNPYEFDSYMIPYNEMNSDGFRLLDVDNRTILPFHTQVRMMVTAADVLHSWTIPALGVKVDATPGRLNQTNFF 160
Cdd:MTH00185 107 SYEYTDY-EQLEFDSYMTPTQDLTPGQFRLLETDHRMVVPMESPIRVLITAEDVLHSWTVPALGVKMDAVPGRLNQATFI 185

                        170
                 ....*....|...
gi 148728385 161 INRPGTYYGQCSE 173
Cdd:MTH00185 186 ISRPGLYYGQCSE 198
COX2 MTH00098
cytochrome c oxidase subunit II; Validated
 1-173 1.94e-69

cytochrome c oxidase subunit II; Validated


Pssm-ID: 177160 [Multi-domain]  Cd Length: 227  Bit Score: 209.96  E-value: 1.94e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148728385   1 TLLILVMITILVAYIMTAIMLYSFTHRYLLEGQLIELIWTILPAMTLIFIALPSLRLLYLLDDTVDPSISLKTVGHQWYW 80
Cdd:MTH00098  27 TLMIVFLISSLVLYIISLMLTTKLTHTSTMDAQEVETIWTILPAIILILIALPSLRILYMMDEINNPSLTVKTMGHQWYW 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148728385  81 SYEYTDFVNpYEFDSYMIPYNEMNSDGFRLLDVDNRTILPFHTQVRMMVTAADVLHSWTIPALGVKVDATPGRLNQTNFF 160
Cdd:MTH00098 107 SYEYTDYED-LSFDSYMIPTSDLKPGELRLLEVDNRVVLPMEMPIRMLISSEDVLHSWAVPSLGLKTDAIPGRLNQTTLM 185

                        170
                 ....*....|...
gi 148728385 161 INRPGTYYGQCSE 173
Cdd:MTH00098 186 STRPGLYYGQCSE 198
COX2 MTH00129
cytochrome c oxidase subunit II; Provisional
 1-173 2.90e-69

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177187 [Multi-domain]  Cd Length: 230  Bit Score: 209.57  E-value: 2.90e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148728385   1 TLLILVMITILVAYIMTAIMLYSFTHRYLLEGQLIELIWTILPAMTLIFIALPSLRLLYLLDDTVDPSISLKTVGHQWYW 80
Cdd:MTH00129  27 ALMIVFLISTLVLYIIVAMVSTKLTNKYILDSQEIEIIWTVLPAVILILIALPSLRILYLMDEINDPHLTIKAMGHQWYW 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148728385  81 SYEYTDFVNpYEFDSYMIPYNEMNSDGFRLLDVDNRTILPFHTQVRMMVTAADVLHSWTIPALGVKVDATPGRLNQTNFF 160
Cdd:MTH00129 107 SYEYTDYED-LGFDSYMIPTQDLTPGQFRLLEADHRMVVPVESPIRVLVSAEDVLHSWAVPALGVKMDAVPGRLNQTAFI 185

                        170
                 ....*....|...
gi 148728385 161 INRPGTYYGQCSE 173
Cdd:MTH00129 186 ASRPGVFYGQCSE 198
COX2 MTH00076
cytochrome c oxidase subunit II; Provisional
 1-173 6.81e-68

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164646 [Multi-domain]  Cd Length: 228  Bit Score: 206.17  E-value: 6.81e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148728385   1 TLLILVMITILVAYIMTAIMLYSFTHRYLLEGQLIELIWTILPAMTLIFIALPSLRLLYLLDDTVDPSISLKTVGHQWYW 80
Cdd:MTH00076  27 ALMAVFLISTLVLYIITIMMTTKLTNTNTMDAQEIEMVWTIMPAIILIVIALPSLRILYLMDEINDPHLTVKAIGHQWYW 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148728385  81 SYEYTDFVNpYEFDSYMIPYNEMNSDGFRLLDVDNRTILPFHTQVRMMVTAADVLHSWTIPALGVKVDATPGRLNQTNFF 160
Cdd:MTH00076 107 SYEYTDYED-LSFDSYMIPTQDLTPGQFRLLEVDNRMVVPMESPIRMLITAEDVLHSWAVPSLGIKTDAIPGRLNQTSFI 185

                        170
                 ....*....|...
gi 148728385 161 INRPGTYYGQCSE 173
Cdd:MTH00076 186 ASRPGVYYGQCSE 198
CcO_II_C cd13912
C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ...
 67-173 9.90e-67

C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal oxidase in the respiratory chains of eukaryotes and most bacteria, is a multi-chain transmembrane protein located in the inner membrane of mitochondria and the cell membrane of prokaryotes. It catalyzes the reduction of O2 and simultaneously pumps protons across the membrane. The number of subunits varies from three to five in bacteria and up to 13 in mammalian mitochondria. Only subunits I and II are essential for function. Subunits I, II, and III of mammalian CcO are encoded within the mitochondrial genome and the remaining 10 subunits are encoded within the nuclear genome. Subunit II contains a copper-copper binuclear site called CuA, which is believed to be involved in electron transfer from cytochrome c to the binuclear center (active site) in subunit I.


Pssm-ID: 259979 [Multi-domain]  Cd Length: 130  Bit Score: 199.72  E-value: 9.90e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148728385  67 PSISLKTVGHQWYWSYEYTDFvNPYEFDSYMIPYNEMNSDGFRLLDVDNRTILPFHTQVRMMVTAADVLHSWTIPALGVK 146
Cdd:cd13912    1 PSLTIKAIGHQWYWSYEYSDF-NDLEFDSYMIPEDDLEKGQLRLLEVDNRLVVPVNTHIRVLVTSADVIHSWAVPSLGIK 79

                         90       100
                 ....*....|....*....|....*..
gi 148728385 147 VDATPGRLNQTNFFINRPGTYYGQCSE 173
Cdd:cd13912   80 VDAVPGRLNQTSFFIERPGVYYGQCSE 106
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
69-173 5.73e-60

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 182.22  E-value: 5.73e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148728385   69 ISLKTVGHQWYWSYEYTDFVNpYEFDSYMIPYNEMNSDGFRLLDVDNRTILPFHTQVRMMVTAADVLHSWTIPALGVKVD 148
Cdd:pfam00116   1 LTIKAIGHQWYWSYEYTDFGD-LEFDSYMIPTEDLEEGQLRLLEVDNRVVLPVETHIRVIVTAADVIHSWAVPSLGIKTD 79

                          90       100
                  ....*....|....*....|....*
gi 148728385  149 ATPGRLNQTNFFINRPGTYYGQCSE 173
Cdd:pfam00116  80 AVPGRLNQTSFSIDREGVFYGQCSE 104
COX2 MTH00027
cytochrome c oxidase subunit II; Provisional
 2-173 1.48e-51

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214405 [Multi-domain]  Cd Length: 262  Bit Score: 165.58  E-value: 1.48e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148728385   2 LLILVMITILVAYIMTAIMLYSFTHRYL---LEGQLIELIWTILPAMTLIFIALPSLRLLYLLDDTV-DPSISLKTVGHQ 77
Cdd:MTH00027  56 LFILTIIVGVVLWLIIRILLGNNYYSYYwnkLDGSLIEVIWTLIPAFILILIAFPSLRLLYIMDECGfSANITIKVTGHQ 135

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148728385  78 WYWSYEYTDFVNP-YEFDSYMIPYNEMNSDGFRLLDVDNRTILPFHTQVRMMVTAADVLHSWTIPALGVKVDATPGRLNQ 156
Cdd:MTH00027 136 WYWSYSYEDYGEKnIEFDSYMIPTADLEFGDLRLLEVDNRLILPVDTNVRVLITAADVLHSWTVPSLAVKMDAVPGRINE 215

                        170
                 ....*....|....*..
gi 148728385 157 TNFFINRPGTYYGQCSE 173
Cdd:MTH00027 216 TGFLIKRPGIFYGQCSE 232
COX2 MTH00080
cytochrome c oxidase subunit II; Provisional
 2-173 2.52e-43

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177149 [Multi-domain]  Cd Length: 231  Bit Score: 143.61  E-value: 2.52e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148728385   2 LLILVMITILVAYIMTAIMLYSFTHRYLL-EGQLIELIWTILPAMTLIFIALPSLRLLYLLDDT-VDPSISLKTVGHQWY 79
Cdd:MTH00080  29 LLFGEFVLAFVVFLFLYLISNNFYFKSKKiEYQFGELLCSVFPVLILLMQMVPSLSLLYYYGLMnLDSNLTVKVTGHQWY 108

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148728385  80 WSYEYTDFVNpYEFDSYMIPYNEMNSDGFRLLDVDNRTILPFHTQVRMMVTAADVLHSWTIPALGVKVDATPGRLNQTNF 159
Cdd:MTH00080 109 WSYEFSDIPG-LEFDSYMKSLDQLRLGEPRLLEVDNRCVLPCDTNIRFCITSSDVIHSWALPSLSIKMDAMSGILSTLCY 187

                        170
                 ....*....|....
gi 148728385 160 FINRPGTYYGQCSE 173
Cdd:MTH00080 188 SFPMPGVFYGQCSE 201
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
1-174 3.38e-34

Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 119.93  E-value: 3.38e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148728385   1 TLLILVMITILVAyIMTAIMLYSFTHR-------YLLEGQLIELIWTILPAMTLIFIALPSLRLLYLLDDTVDPSISLKT 73
Cdd:COG1622   39 SLIIMLVIFVLVF-GLLLYFAIRYRRRkgdadpaQFHHNTKLEIVWTVIPIIIVIVLAVPTLRVLHALDDAPEDPLTVEV 117

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148728385  74 VGHQWYWSYEYTDfvnpyefdsymipYNEmnsdgfrllDVDNRTILPFHTQVRMMVTAADVLHSWTIPALGVKVDATPGR 153
Cdd:COG1622  118 TGYQWKWLFRYPD-------------QGI---------ATVNELVLPVGRPVRFLLTSADVIHSFWVPALGGKQDAIPGR 175

                        170       180
                 ....*....|....*....|.
gi 148728385 154 LNQTNFFINRPGTYYGQCSEF 174
Cdd:COG1622  176 VTELWFTADKPGTYRGQCAEL 196
PTZ00047 PTZ00047
cytochrome c oxidase subunit II; Provisional
 91-173 1.93e-29

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 240243 [Multi-domain]  Cd Length: 162  Bit Score: 106.06  E-value: 1.93e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148728385  91 YEFDSYMIPYNEMNSDGFRLLDVDNRTILPFHTQVRMMVTAADVLHSWTIPALGVKVDATPGRLNQTNFFINRPGTYYGQ 170
Cdd:PTZ00047  49 YSFQSNLVTDEDLKPGMLRQLEVDKRLTLPTRTHIRFLITATDVIHSWSVPSLGIKADAIPGRLHKINTFILREGVFYGQ 128


                 ...
gi 148728385 171 CSE 173
Cdd:PTZ00047 129 CSE 131
COX2 MTH00047
cytochrome c oxidase subunit II; Provisional
 31-174 3.03e-29

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214412 [Multi-domain]  Cd Length: 194  Bit Score: 106.19  E-value: 3.03e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148728385  31 EGQLIELIWTILPAMTLIFIALPSLRLLYLLDDTVdPSISLKTVGHQWYWSYEYtdfVNPYEFDSYMipynemNSDGFrl 110
Cdd:MTH00047  45 ENQVLELLWTVVPTLLVLVLCFLNLNFITSDLDCF-SSETIKVIGHQWYWSYEY---SFGGSYDSFM------TDDIF-- 112

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 148728385 111 lDVDNRTILPFHTQVRMMVTAADVLHSWTIPALGVKVDATPGRLNQTNFFINRPGTYYGQCSEF 174
Cdd:MTH00047 113 -GVDKPLRLVYGVPYHLLVTSSDVIHSFSVPDLNLKMDAIPGRINHLFFCPDRHGVFVGYCSEL 175
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 2-174 2.99e-25

cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of mitochondria (and one of several possible acceptors in prokaryotes) in the electron transport chain of aerobic respiration. The enzyme couples the oxidation of reduced cytochrome c with the reduction of molecular oxygen to water. This process results in the pumping of four protons across the membrane which are used in the proton gradient powered synthesis of ATP. The oxidase contains two heme a cofactors and three copper atoms as well as other bound ions. [Energy metabolism, Electron transport]


Pssm-ID: 274329 [Multi-domain]  Cd Length: 199  Bit Score: 96.30  E-value: 2.99e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148728385    2 LLILVMITILVayIMTAIMLYS-FTHR---------YLLEGQLIELIWTILPA-MTLIFIALPSLRLLYLLDDTVDPSIS 70
Cdd:TIGR02866  15 FVLAVSTLISL--LVAALLAYVvWKFRrkgdeekpsQIHGNRRLEYVWTVIPLiIVVGLFAATAKGLLYLERPIPKDALK 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148728385   71 LKTVGHQWYWSYEYTDFvnpyefdsymipynemnsdGFRlldVDNRTILPFHTQVRMMVTAADVLHSWTIPALGVKVDAT 150
Cdd:TIGR02866  93 VKVTGYQWWWDFEYPES-------------------GFT---TVNELVLPAGTPVELQVTSKDVIHSFWVPELGGKIDAI 150

                         170       180
                  ....*....|....*....|....
gi 148728385  151 PGRLNQTNFFINRPGTYYGQCSEF 174
Cdd:TIGR02866 151 PGQTNALWFNADEPGVYYGFCAEL 174
CuRO_HCO_II_like cd13842
Cupredoxin domain of Heme-copper oxidase subunit II; Heme-copper oxidases are transmembrane ...
 72-174 1.92e-18

Cupredoxin domain of Heme-copper oxidase subunit II; Heme-copper oxidases are transmembrane protein complexes in the respiratory chains of prokaryotes and mitochondria which catalyze the reduction of O2 and simultaneously pump protons across the membrane. The superfamily is diverse in terms of electron donors, subunit composition, and heme types. The number of subunits varies from two to five in bacteria and up to 13 in mammalian mitochondria. Subunits I, II, and III of mammalian cytochrome c oxidase (CcO) are encoded within the mitochondrial genome and the remaining 10 subunits are encoded within the nuclear genome. It has been proposed that archaea acquired heme-copper oxidases through gene transfer from gram-positive bacteria. Subunit II is found in CcO, ubiquinol oxidase, and the ba3-like oxidases, while the cbb3 oxidases contain alternative additional subunits. Additionally, nitrous oxide reductase contains the globular portion of subunit II as a domain within its structure. In some families, subunit II contains a copper-copper binuclear center that is involved in the transfer of electrons from the substrate to the binuclear center (active site) in subunit I.


Pssm-ID: 259911 [Multi-domain]  Cd Length: 95  Bit Score: 75.80  E-value: 1.92e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148728385  72 KTVGHQWYWSYEYTDfvnpyefdsymipynemnsdgfrlLDVDNRTILPFHTQVRMMVTAADVLHSWTIPALGVKVDATP 151
Cdd:cd13842    4 YVTGVQWSWTFIYPN------------------------VRTPNEIVVPAGTPVRFRVTSPDVIHGFYIPNLGVKVDAVP 59

                         90       100
                 ....*....|....*....|...
gi 148728385 152 GRLNQTNFFINRPGTYYGQCSEF 174
Cdd:cd13842   60 GYTSELWFVADKPGTYTIICAEY 82
CuRO_CcO_Caa3_II cd04213
The cupredoxin domain of Caa3 type Cytochrome c oxidase subunit II; Cytochrome c oxidase (CcO), ...
 71-174 9.34e-17

The cupredoxin domain of Caa3 type Cytochrome c oxidase subunit II; Cytochrome c oxidase (CcO), the terminal oxidase in the respiratory chains of most bacteria, is a multi-chain transmembrane protein located in the inner membrane the cell membrane of prokaryotes. It catalyzes the reduction of O2 and simultaneously pumps protons across the membrane. Caa3 type of CcO Subunit II contains a copper-copper binuclear site called CuA, which is believed to be involved in electron transfer from cytochrome c to the cytochromes a, a3 and CuB active site in subunit I.


Pssm-ID: 259875 [Multi-domain]  Cd Length: 103  Bit Score: 71.50  E-value: 9.34e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148728385  71 LKTVGHQWYWSYEYTDfvnpyefdsymipynemnSDGFRLLDVdNRTILPFHTQVRMMVTAADVLHSWTIPALGVKVDAT 150
Cdd:cd04213    4 IEVTGHQWWWEFRYPD------------------EPGRGIVTA-NELHIPVGRPVRLRLTSADVIHSFWVPSLAGKMDMI 64

                         90       100
                 ....*....|....*....|....
gi 148728385 151 PGRLNQTNFFINRPGTYYGQCSEF 174
Cdd:cd04213   65 PGRTNRLWLQADEPGVYRGQCAEF 88
CuRO_HCO_II_like_5 cd13919
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 72-174 2.75e-13

Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; Heme-copper oxidases are transmembrane protein complexes in the respiratory chains of prokaryotes and mitochondria which catalyze the reduction of O2 and simultaneously pump protons across the membrane. The superfamily is diverse in terms of electron donors, subunit composition, and heme types. The number of subunits varies from two to five in bacteria and up to 13 in mammalian mitochondria. Subunits I, II, and III of mammalian cytochrome c oxidase (CcO) are encoded within the mitochondrial genome and the remaining 10 subunits are encoded within the nuclear genome. It has been proposed that archaea acquired heme-copper oxidases through gene transfer from gram-positive bacteria. Subunit II is found in CcO, ubiquinol oxidase, and the ba3-like oxidases, while the cbb3 oxidases contain alternative additional subunits. Additionally, nitrous oxide reductase contains the globular portion of subunit II as a domain within its structure. In some families, subunit II contains a copper-copper binuclear center that is involved in the transfer of electrons from the substrate to the binuclear center (active site) in subunit I.


Pssm-ID: 259986 [Multi-domain]  Cd Length: 107  Bit Score: 62.66  E-value: 2.75e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148728385  72 KTVGHQWYWSYEYTDFVNPYEFDSyMIPYNEMNsdgfrlldvdnrtiLPFHTQVRMMVTAADVLHSWTIPALGVKVDATP 151
Cdd:cd13919    5 EVTAQQWAWTFRYPGGDGKLGTDD-DVTSPELH--------------LPVGRPVLFNLRSKDVIHSFWVPEFRVKQDAVP 69

                         90       100
                 ....*....|....*....|...
gi 148728385 152 GRLNQTNFFINRPGTYYGQCSEF 174
Cdd:cd13919   70 GRTTRLWFTPTREGEYEVRCAEL 92
CuRO_HCO_II_like_2 cd13915
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 74-174 6.85e-13

Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; Heme-copper oxidases are transmembrane protein complexes in the respiratory chains of prokaryotes and mitochondria which catalyze the reduction of O2 and simultaneously pump protons across the membrane. The superfamily is diverse in terms of electron donors, subunit composition, and heme types. The number of subunits varies from two to five in bacteria and up to 13 in mammalian mitochondria. Subunits I, II, and III of mammalian cytochrome c oxidase (CcO) are encoded within the mitochondrial genome and the remaining 10 subunits are encoded within the nuclear genome. It has been proposed that archaea acquired heme-copper oxidases through gene transfer from gram-positive bacteria. Subunit II is found in CcO, ubiquinol oxidase, and the ba3-like oxidases, while the cbb3 oxidases contain alternative additional subunits. Additionally, nitrous oxide reductase contains the globular portion of subunit II as a domain within its structure. In some families, subunit II contains a copper-copper binuclear center that is involved in the transfer of electrons from the substrate to the binuclear center (active site) in subunit I.


Pssm-ID: 259982 [Multi-domain]  Cd Length: 98  Bit Score: 61.49  E-value: 6.85e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148728385  74 VGHQWYWSYEYtdfvnpyefdsymipynemnSDGFRlldVDNRTILPFHTQVRMMVTAADVLHSWTIPALGVKVDATPGR 153
Cdd:cd13915    7 TGRQWMWEFTY--------------------PNGKR---EINELHVPVGKPVRLILTSKDVIHSFYVPAFRIKQDVVPGR 63

                         90       100
                 ....*....|....*....|.
gi 148728385 154 LNQTNFFINRPGTYYGQCSEF 174
Cdd:cd13915   64 YTYLWFEATKPGEYDLFCTEY 84
CuRO_HCO_II_like_3 cd13914
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 74-174 2.68e-12

Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; Heme-copper oxidases are transmembrane protein complexes in the respiratory chains of prokaryotes and mitochondria which catalyze the reduction of O2 and simultaneously pump protons across the membrane. The superfamily is diverse in terms of electron donors, subunit composition, and heme types. The number of subunits varies from two to five in bacteria and up to 13 in mammalian mitochondria. Subunits I, II, and III of mammalian cytochrome c oxidase (CcO) are encoded within the mitochondrial genome and the remaining 10 subunits are encoded within the nuclear genome. It has been proposed that archaea acquired heme-copper oxidases through gene transfer from gram-positive bacteria. Subunit II is found in CcO, ubiquinol oxidase, and the ba3-like oxidases, while the cbb3 oxidases contain alternative additional subunits. Additionally, nitrous oxide reductase contains the globular portion of subunit II as a domain within its structure. In some families, subunit II contains a copper-copper binuclear center that is involved in the transfer of electrons from the substrate to the binuclear center (active site) in subunit I.


Pssm-ID: 259981 [Multi-domain]  Cd Length: 108  Bit Score: 60.11  E-value: 2.68e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148728385  74 VGHQWYWSYEYtdfvnpyefdsymipyNEMNSDGFrlldvdNRTILPFHTQVRMMVTAADVLHSWTIPALGVKVDATPGR 153
Cdd:cd13914    6 EAYQWGWEFSY----------------PEANVTTS------EQLVIPADRPVYFRITSRDVIHAFHVPELGLKQDAFPGQ 63

                         90       100
                 ....*....|....*....|.
gi 148728385 154 LNQTNFFINRPGTYYGQCSEF 174
Cdd:cd13914   64 YNTIKTEATEEGEYQLYCAEY 84
CuRO_HCO_II_like_6 cd13918
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 62-173 2.09e-11

Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; Heme-copper oxidases are transmembrane protein complexes in the respiratory chains of prokaryotes and mitochondria which catalyze the reduction of O2 and simultaneously pump protons across the membrane. The superfamily is diverse in terms of electron donors, subunit composition, and heme types. The number of subunits varies from two to five in bacteria and up to 13 in mammalian mitochondria. Subunits I, II, and III of mammalian cytochrome c oxidase (CcO) are encoded within the mitochondrial genome and the remaining 10 subunits are encoded within the nuclear genome. It has been proposed that archaea acquired heme-copper oxidases through gene transfer from gram-positive bacteria. Subunit II is found in CcO, ubiquinol oxidase, and the ba3-like oxidases, while the cbb3 oxidases contain alternative additional subunits. Additionally, nitrous oxide reductase contains the globular portion of subunit II as a domain within its structure. In some families, subunit II contains a copper-copper binuclear center that is involved in the transfer of electrons from the substrate to the binuclear center (active site) in subunit I.


Pssm-ID: 259985 [Multi-domain]  Cd Length: 139  Bit Score: 58.62  E-value: 2.09e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148728385  62 DDTVDPSISLKTVGHQWYWSYEYTdfvNPYEFDSYMIpynemnsdgfrlldvdnrtiLPFHTQVRMMVTAADVLHSWTIP 141
Cdd:cd13918   26 DEADEDALEVEVEGFQFGWQFEYP---NGVTTGNTLR--------------------VPADTPIALRVTSTDVFHTFGIP 82

                         90       100       110
                 ....*....|....*....|....*....|..
gi 148728385 142 ALGVKVDATPGRLNQTNFFINRPGTYYGQCSE 173
Cdd:cd13918   83 ELRVKADAIPGEYTSTWFEADEPGTYEAKCYE 114
COX2_TM pfam02790
Cytochrome C oxidase subunit II, transmembrane domain; The N-terminal domain of cytochrome C ...
 1-51 3.46e-10

Cytochrome C oxidase subunit II, transmembrane domain; The N-terminal domain of cytochrome C oxidase contains two transmembrane alpha-helices.


Pssm-ID: 397083 [Multi-domain]  Cd Length: 89  Bit Score: 53.87  E-value: 3.46e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 148728385    1 TLLILVMITILVAYIM-TAIMLY-----SFTHRYLLEGQLIELIWTILPAMTLIFIA 51
Cdd:pfam02790  27 IMFILTLILILVLYILvTCLIRFnrrknPITARYTTHGQTIEIIWTIIPAVILILIA 83
CuRO_UO_II cd04212
The cupredoxin domain of Ubiquinol oxidase subunit II; Ubiquinol oxidase, the terminal oxidase ...
 115-174 1.69e-07

The cupredoxin domain of Ubiquinol oxidase subunit II; Ubiquinol oxidase, the terminal oxidase in the respiratory chains of aerobic bacteria, is a multi-chain transmembrane protein located in the cell membrane. It catalyzes the reduction of O2 and simultaneously pumps protons across the membrane. The number of subunits in ubiquinol oxidase varies from two to five. Although subunit II of ubiquinol oxidase lacks the binuclear CuA site found in cytochrome c oxidases, the structure is conserved.


Pssm-ID: 259874 [Multi-domain]  Cd Length: 99  Bit Score: 47.16  E-value: 1.69e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 148728385 115 NRTILPFHTQVRMMVTAADVLHSWTIPALGVKVDATPGRLNQTNFFINRPGTYYGQCSEF 174
Cdd:cd04212   25 NELVIPVGRPVNFRLTSDSVMNSFFIPQLGGQIYAMAGMQTQLHLIADKPGTYQGLSANY 84
ba3_CcO_II_C cd13913
C-terminal cupredoxin domain of Ba3-like heme-copper oxidase subunit II; The ba3 family of ...
 119-174 6.34e-05

C-terminal cupredoxin domain of Ba3-like heme-copper oxidase subunit II; The ba3 family of heme-copper oxidases are transmembrane protein complexes in the respiratory chains of prokaryotes and some archaea, which catalyze the reduction of O2 and simultaneously pump protons across the membrane. It has been proposed that archaea acquired heme-copper oxidases through gene transfer from gram-positive bacteria. The ba3 family contains oxidases that lack the conserved residues that form the D- and K-pathways in CcO and ubiquinol oxidase. Instead, they contain a potential alternative K-pathway. Additional proton channels have been proposed for this family of oxidases but none have been identified definitively.


Pssm-ID: 259980 [Multi-domain]  Cd Length: 99  Bit Score: 40.25  E-value: 6.34e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 148728385 119 LPFHTQVRMMVTAADVLHSWTIPALGVKVDATPGRLNQTNFFINRPGTYYGQCSEF 174
Cdd:cd13913   29 VPAGATVTFYVTSKDVIHGFEIAGTNVNVMVIPGQVSSVTYTFDKPGEYLIICNEY 84
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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